CAZyme Information: MGYG000004314_01510

Basic Information

• Species: Varibaculum timonense
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Actinomycetaceae; Varibaculum; Varibaculum timonense
• CAZyme ID: MGYG000004314_01510
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1212	MGYG000004314_16|CGC1	129636.95	6.3111

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004314	2027678	MAG	Israel	Asia

• Gene Location: Start: 127; End: 3765 Strand: +

Full Sequence      

MLLQKRKTPSVSSWVKADKTGKGRQRIGSKLLKPLGVALVSGALALSISLPAPMAQAEPL
GAYKADGSATLPKTIPSLDAWKASGGTWTLAEGARVVSTQELNARAKSLSTELSAYLGSP
VPAKIGKRTSEFDVQLLQDSTRKDLGAEGFELKIGSSGVQIIGATDAGVFYGTRSFSQLM
RQKQLTLPAGSVISVPKYKERGVTLCACQLNISTEWIERFLDDAADLHINNIVLEMKLKS
DAYPDTQTWSYYTPEDVKKFVAKAKSLNIDVIPEINSPGHMNIWLENAPQYQLVDKNGGY
HPDQLDISNPKARAFIKKLIDEYDGAFDSKFWHMGADEYTMTGGYQLYPQLTKYAQDAFG
PSANANDAFTAFINEINTYVKGKGKNLRIFNDGLYDTANVQLDKDIIIDYWFKKGGTLTP
QQLAERGYQLTNVPQAMYWSRAFDPAGYTYAMKPNNLYNNKNWNVGTFDGGAQIDPNYDK
LLGARVSLWPDNINETENEVQMITADSLRFLAQMTWSASRPWPKWEGADGMKATIDSLGD
PTTRSQVQAATVPDGVYGLPELDPVANGPWKLAKTYDGYYQISNAATGKCLTMSEGAKHL
GAVSEVGAQPTLVSCRPLSETYKNAFAAGRERNQQKWQVVVEADNKVSLRNAVSIQYLAV
ADGSEKHVDIQGVSAAEVKADATLLEKSLSKTGNNLAAGKVAQFPKDLVATKGKLADKAL
FSLVREKSITVDQPEIKDVNPSEPREVTVTVSAADNAKVAPSEIKATVSEGWKVLPETVQ
IGELPARGTGTAKFKLVNTTGTTGTATFTWKMGNEELSTTVKLSGMLGPRVCDGFTDLSA
DSEEKTGEGATNGHVKAAFDGVDESGKSNTFWHSKWSGGVDSLPHWLVFSPQQALTNPDG
TINNMLSVEYLSRQGKVNGRIKSYQIYTSDTTKDGNATTGWTLQKEGQWENGTDWQRAYY
DNPVKAKYVKLLITDVWDEVAGTEDQFASAAAICVSSQMPPATLTAPAQPENPISVSPAV
KVQNAPANPWPAADPAAPAATIAAIADQSLQLGAAIKDIPVKVANGTVREVKGLPAGVVF
DKQTGVISGKPAKAGKYSVQVIAENPDEEEVTAAFTITVTEENTPGDTGKPGGSDKPGDT
GKPGTSDKPAPGGNASGDGKGKAPGSAAPAGNGNGQASSPGLEGTGSNAAIMLGAALLLI
AAGTVAIKRRRL

Enzyme Prediction     

EC	3.2.1.97	3.2.1.140

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH20	196	518	2.5e-55	0.9643916913946587

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06564	GH20_DspB_LnbB-like	1.26e-67	199	516	1	324	Glycosyl hydrolase family 20 (GH20) catalytic domain of dispersin B (DspB), lacto-N-biosidase (LnbB) and related proteins. Dispersin B is a soluble beta-N-acetylglucosamidase found in bacteria that hydrolyzes the beta-1,6-linkages of PGA (poly-beta-(1,6)-N-acetylglucosamine), a major component of the extracellular polysaccharide matrix. Lacto-N-biosidase hydrolyzes lacto-N-biose (LNB) type I oligosaccharides at the nonreducing terminus to produce lacto-N-biose as part of the GNB/LNB (galacto-N-biose/lacto-N-biose I) degradation pathway. The lacto-N-biosidase from Bifidobacterium bifidum has this GH20 domain, a carbohydrate binding module 32, and a bacterial immunoglobulin-like domain 2, as well as a YSIRK signal peptide and a G5 membrane anchor at the N and C termini, respectively. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself.
cd02742	GH20_hexosaminidase	2.60e-30	212	517	13	303	Beta-N-acetylhexosaminidases of glycosyl hydrolase family 20 (GH20) catalyze the removal of beta-1,4-linked N-acetyl-D-hexosamine residues from the non-reducing ends of N-acetyl-beta-D-hexosaminides including N-acetylglucosides and N-acetylgalactosides. These enzymes are broadly distributed in microorganisms, plants and animals, and play roles in various key physiological and pathological processes. These processes include cell structural integrity, energy storage, cellular signaling, fertilization, pathogen defense, viral penetration, the development of carcinomas, inflammatory events and lysosomal storage disorders. The GH20 enzymes include the eukaryotic beta-N-acetylhexosaminidases A and B, the bacterial chitobiases, dispersin B, and lacto-N-biosidase. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by the solvent or the enzyme, but by the substrate itself.
pfam00728	Glyco_hydro_20	1.54e-25	244	518	67	345	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd06563	GH20_chitobiase-like	2.46e-20	251	438	82	266	The chitobiase of Serratia marcescens is a beta-N-1,4-acetylhexosaminidase with a glycosyl hydrolase family 20 (GH20) domain that hydrolyzes the beta-1,4-glycosidic linkages in oligomers derived from chitin. Chitin is degraded by a two step process: i) a chitinase hydrolyzes the chitin to oligosaccharides and disaccharides such as di-N-acetyl-D-glucosamine and chitobiose, ii) chitobiase then further degrades these oligomers into monomers. This GH20 domain family includes an N-acetylglucosamidase (GlcNAcase A) from Pseudoalteromonas piscicida and an N-acetylhexosaminidase (SpHex) from Streptomyces plicatus. SpHex lacks the C-terminal PKD (polycystic kidney disease I)-like domain found in the chitobiases. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself.
cd06562	GH20_HexA_HexB-like	8.46e-20	242	430	60	244	Beta-N-acetylhexosaminidases catalyze the removal of beta-1,4-linked N-acetyl-D-hexosamine residues from the non-reducing ends of N-acetyl-beta-D-hexosaminides including N-acetylglucosides and N-acetylgalactosides. The hexA and hexB genes encode the alpha- and beta-subunits of the two major beta-N-acetylhexosaminidase isoenzymes, N-acetyl-beta-D-hexosaminidase A (HexA) and beta-N-acetylhexosaminidase B (HexB). Both the alpha and the beta catalytic subunits have a TIM-barrel fold and belong to the glycosyl hydrolase family 20 (GH20). The HexA enzyme is a heterodimer containing one alpha and one beta subunit while the HexB enzyme is a homodimer containing two beta-subunits. Hexosaminidase mutations cause an inability to properly hydrolyze certain sphingolipids which accumulate in lysosomes within the brain, resulting in the lipid storage disorders Tay-Sachs and Sandhoff. Mutations in the alpha subunit cause in a deficiency in the HexA enzyme and result in Tay-Sachs, mutations in the beta-subunit cause in a deficiency in both HexA and HexB enzymes and result in Sandhoff disease. In both disorders GM(2) gangliosides accumulate in lysosomes. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QTG76252.1	0.0	37	1014	14	1001
QOQ38946.1	0.0	37	1014	14	1001
QOR46426.1	0.0	37	1014	14	1001
AXM91224.1	1.61e-260	70	1132	51	1063
BBA47460.1	1.74e-259	70	1132	51	1062

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4H04_A	1.86e-220	70	710	32	643	Lacto-N-biosidasefrom Bifidobacterium bifidum [Bifidobacterium bifidum JCM 1254],4H04_B Lacto-N-biosidase from Bifidobacterium bifidum [Bifidobacterium bifidum JCM 1254],4JAW_A Crystal Structure of Lacto-N-Biosidase from Bifidobacterium bifidum complexed with LNB-thiazoline [Bifidobacterium bifidum JCM 1254],4JAW_B Crystal Structure of Lacto-N-Biosidase from Bifidobacterium bifidum complexed with LNB-thiazoline [Bifidobacterium bifidum JCM 1254],5BXP_A LNBase in complex with LNB-LOGNAc [Bifidobacterium bifidum JCM 1254],5BXP_B LNBase in complex with LNB-LOGNAc [Bifidobacterium bifidum JCM 1254],5BXR_A LNBase in complex with LNB-NHAcDNJ [Bifidobacterium bifidum JCM 1254],5BXR_B LNBase in complex with LNB-NHAcDNJ [Bifidobacterium bifidum JCM 1254],5BXS_A LNBase in complex with LNB-NHAcCAS [Bifidobacterium bifidum JCM 1254],5BXS_B LNBase in complex with LNB-NHAcCAS [Bifidobacterium bifidum JCM 1254],5BXT_A LNBase in complex with LNB-NHAcAUS [Bifidobacterium bifidum JCM 1254],5BXT_B LNBase in complex with LNB-NHAcAUS [Bifidobacterium bifidum JCM 1254]
7DUP_A	4.23e-21	124	439	56	415	ChainA, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVA_A Chain A, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVA_B Chain B, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron]
6JQF_A	6.44e-21	72	520	89	550	Crystallizationanalysis of a beta-N-acetylhexosaminidase (Am2136) from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835]
7DVB_A	1.74e-20	124	439	56	415	ChainA, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVB_B Chain B, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVB_C Chain C, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVB_D Chain D, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron]
4AZ7_A	1.09e-19	199	491	6	339	Differentialinhibition of the tandem GH20 catalytic modules in the pneumococcal exo-beta-D-N-acetylglucosaminidase, StrH [Streptococcus pneumoniae TIGR4]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B2UPR7	8.57e-23	72	520	111	572	Beta-hexosaminidase Amuc_2136 OS=Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP 107961 / Muc) OX=349741 GN=Amuc_2136 PE=1 SV=1
Q04786	1.85e-20	86	526	212	723	Beta-hexosaminidase OS=Vibrio vulnificus OX=672 GN=hex PE=3 SV=1
P13723	3.69e-18	134	502	86	456	Beta-hexosaminidase subunit A1 OS=Dictyostelium discoideum OX=44689 GN=hexa1 PE=1 SV=1
P49610	7.64e-18	242	439	704	903	Beta-N-acetylhexosaminidase OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=strH PE=1 SV=2
P49008	3.25e-16	97	338	61	335	Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.091636	0.887464	0.015378	0.004738	0.000514	0.000257

TMHMM  Annotations     

start	end
1185	1207